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Database: UniProt
Entry: K2DZR6_9BACT
LinkDB: K2DZR6_9BACT
Original site: K2DZR6_9BACT 
ID   K2DZR6_9BACT            Unreviewed;       501 AA.
AC   K2DZR6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=ACD_20C00357G0025 {ECO:0000313|EMBL:EKE02602.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE02602.1};
RN   [1] {ECO:0000313|EMBL:EKE02602.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKE02602.1}.
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DR   EMBL; AMFJ01007836; EKE02602.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2DZR6; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF3; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          12..147
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          162..464
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          469..496
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   501 AA;  57247 MW;  CE296FEAFA45962C CRC64;
     MTTQEEIRQE KINSTIWKAC DTFRGVVDPS EYKNYILVFL FLKYLSDSWK EKLEKCKEEF
     GDDKERTNRR MSRERFTLPE NCSFDYIYSM RNEDNIGEII NQALDGIEEA NKAKLENVFR
     NIDFNSESNL GETKDRNTRL KNLIEDFADK ELDLRPSRIG NNDIIGNVYE YLIARFASGA
     GKKGGEFYTP AEVAILLAKL LKAQPGDRIS DPTAGSGSLL IRVAREIGNS DFSLYGQESN
     GSTWALCKMN MFLHEMDNAR IEWGDTLRNP KLLENDKLMK FDIVVSNPPF SLDKWGADVA
     EADDYNRFHR GIPPKSKADY AFITHMIETS TEGTGKVGVI VPHGVLFRES SEGKIRRQLI
     EENLLEAVIG LPQNLFYGTG IPAAILIFNK GKTTKDVLFI DGSRQYEAGK NQNKLSDKNI
     NDIVEVYTKG ETRDKYSYKA TYQEIVDNEY NLNIPRYVDT FEEEGEISIT DVQKQINSLE
     SELLQVRQEM QGYLEELGLK V
//
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